The Scavenger Receptor SSc5D Physically Interacts with Bacteria through the SRCR-Containing N-Terminal Domain

0469630 - ÚFE 2017 RIV CH eng J - Journal Article
Pereira, C.B. - Bocková, Markéta - Santos, R.F. - Santos, A. M. - de Araujo, M.M. - Oliveira, L. - Homola, Jiří - Carmo, A.M.
The Scavenger Receptor SSc5D Physically Interacts with Bacteria through the SRCR-Containing N-Terminal Domain.
Frontiers in Immunology. Roč. 7, October (2016), č. článku 416. ISSN 1664-3224. E-ISSN 1664-3224
R&D Projects: GA ČR(CZ) GBP205/12/G118
Grant - others:AV ČR(CZ) AP1101
Program: Akademická prémie - Praemium Academiae
Institutional support: RVO:67985882
Keywords : Pattern recognition receptors * Bacteria * Surface plasmon resonance
Subject RIV: BH - Optics, Masers, Lasers
Impact factor: 6.429, year: 2016

The scavenger receptor cysteine-rich (SRCR) family comprises a group of membrane-attached or secreted proteins that contain one or more modules/domains structurally similar to the membrane distal domain of type I macrophage scavenger receptor. Although no all-inclusive biological function has been ascribed to the SRCR family, some of these receptors have been shown to recognize pathogen-associated molecular patterns (PAMP) of bacteria, fungi, or other microbes. SSc5D is a recently described soluble SRCR receptor produced by monocytes/macrophages and T lymphocytes, consisting of an N-terminal portion, which contains five SRCR modules, and a large C-terminal mucin-like domain. Toward establishing a global common role for SRCR domains, we interrogated whether the set of five SRCR domains of SSc5D displayed pattern recognition receptor (PRR) properties. For that purpose, we have expressed in a mammalian expression system the N-terminal SRCR-containing moiety of SSc5D (N-SSc5D), thus excluding the mucin-like domain likely by nature to bind microorganisms, and tested the capacity of the SRCR functional groups to physically interact with bacteria. Using conventional protein-bacteria binding assays, we showed that N-SSc5D had a superior capacity to bind to Escherichia coli strains RS218 and IHE3034 compared with that of the extracellular domains of the SRCR proteins CD5 and CD6 (sCD5 and sCD6, respectively), and similar E. coli-binding properties as Spa, a proven PRR of the SRCR family. We have further designed a more sensitive, real-time, and label-free surface plasmon resonance (SPR)-based assay and examined the capacity of N-SSc5D, Spa, sCD5, and sCD6 to bind to different bacteria. We demonstrated that N-SSc5D compares with Spa in the capacity to bind to E. coli and Listeria monocytogenes, and further that it can distinguish between pathogenic E. coli RS218 and IHE3034 strains and the non-pathogenic laboratory E. coli strain BL21(DE3).
Permanent Link: http://hdl.handle.net/11104/0267454